This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1kwk

From Proteopedia

Revision as of 23:57, 24 November 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

1kwk, resolution 2.20Å

Drag the structure with the mouse to rotate

Crystal structure of Thermus thermophilus A4 beta-galactosidase in complex with galactose

Overview

The beta-galactosidase from an extreme thermophile, Thermus thermophilus, A4 (A4-beta-Gal), is thermostable and belongs to the glycoside hydrolase, family 42 (GH-42). As the first known structures of a GH-42 enzyme, we, determined the crystal structures of free and galactose-bound A4-beta-Gal, at 1.6A and 2.2A resolution, respectively. A4-beta-Gal forms a, homotrimeric structure resembling a flowerpot. Each monomer has an active, site located inside a large central tunnel. The N-terminal domain of, A4-beta-Gal has a TIM barrel fold, as predicted from hydrophobic cluster, analysis. The putative catalytic residues of A4-beta-Gal (Glu141 and, Glu312) superimpose well with the catalytic residues of Escherichia coli, beta-galactosidase. The environment around the catalytic nucleophile, (Glu312) is similar to that in the case of E.coli beta-galactosidase, but, the recognition mechanism for a substrate is different. Trp182 of the next, subunit of the trimer constitutes a part of the active-site pocket, indicating that the trimeric structure is essential for the enzyme, activity. Structural comparison with other glycoside hydrolases revealed, that many features of the 4/7 superfamily are conserved in the A4-beta-Gal, structure. On the basis of the results of 1H NMR spectroscopy, A4-beta-Gal, was determined to be a "retaining" enzyme. Interestingly, the active site, was similar with those of retaining enzymes, but the overall fold of the, TIM barrel domain was very similar to that of an inverting enzyme, beta-amylase.

About this Structure

1KWK is a Single protein structure of sequence from Thermus thermophilus with GAL, CL, ACT, ZN and MPD as ligands. Active as Beta-galactosidase, with EC number 3.2.1.23 Full crystallographic information is available from OCA.

Reference

Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose., Hidaka M, Fushinobu S, Ohtsu N, Motoshima H, Matsuzawa H, Shoun H, Wakagi T, J Mol Biol. 2002 Sep 6;322(1):79-91. PMID:12215416

Page seeded by OCA on Sun Nov 25 02:05:18 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools